Related Sites

Peter Martin

NHH 5-290 (lab)
pmartin @ physics.umn.edu

I am a graduate student here at the School of Physics and Astronomy. I started graduate school by working with Professor Michael Zudov and studying nonequilibrium transport in high mobility two dimensional electron gases. While the physics certainly was interesting, after a few years, I decided that life at high vacuum and below 4 K was not for me, so I finished up some of my work, earning my M.S. and contributing to a few publications in the process. I then decided to make a big switch to biophysics, and now I study membrane proteins using EPR spectroscopy under Professor David Thomas, who has an appointment in the Biochemistry, Molecular Biology, and Biophysics Department. Not having taken any chemistry courses since high school, I certainly have had my work cut out for me in exploring what biophysics has to offer, but I am thoroughly enjoying the challenge. Working with an adviser and students in a biochemistry department has offered me new perspectives on how to approach the complexity behind the physics of living systems. In addition, I have offered them a unique skill set by bringing my background of physics, mathematics, and experience with instrumentation.

Summary of Interests

Molecular biophysics of membrane proteins and lipid membranes

About My Work

A number of studies on patients who experienced heart failure have shown low calcium pump activity inside their cardiac muscle tissue. The membrane proteins that are primarily responsible for controlling Ca2+ concentration inside muscle cells are the ryanodine receptor (RyR), and the sarcoplasmic reticulum Ca2+-ATPase (SERCA). Upon binding to SERCA, the small membrane protein phospholamban (PLB) has been shown to greatly inhibit SERCA’s activity. However, SERCA activity can be partially restored upon phosphorylation of PLB or elevated Ca2+ concentration (several micromolar) in the cytosol. To better understand the structural mechanisms behind these phenomena, I employ electron paramagnetic resonance spectroscopy in conjunction with site-directed spin labeling on PLB and SERCA.